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  • Title: GTP, as well as ATP, can act as a substrate for the intrinsic protein kinase activity of synaptic plasma membranes.
    Author: Weller M, Haag M, Laing W.
    Journal: Mol Cell Biochem; 1981 Oct 30; 40(2):75-85. PubMed ID: 7311972.
    Abstract:
    GTP as well as ATP can act as phosphate donor for the intrinsic protein kinase activity of synaptic plasma membranes. There are many similarities between the activities observed with ATP or GTP. Both need a divalent cation, Mg2+ being preferred, both are slightly inhibited by Na+, and more strongly by K+, both are inhibited by theophylline and adenosine. The Km for GTP (0.13 mM) is similar to that ATP (0.12 mM). There are, however, some differences in properties. When GTP instead of ATP is the phosphate donor the pH optimum is 6.5 instead of 7.4. In addition NH4+ inhibits the transfer of phosphate from GTP but not from ATP. More importantly, cyclic AMP only stimulates the transfer of phosphate from ATP not from GTP. SDS gel electrophoresis reveals that similar membrane proteins are phosphorylated by GTP and ATP in the presence or absence of cyclic AMP. This suggests that there may be two different types of protein kinase in the synaptic plasma membrane which act on similar membrane proteins. One is stimulated by cyclic AMP and is specific to ATP while the other is unaffected by cyclic nucleotides and can use either ATP or GTP as phosphate donor.
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